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Biochemistry|June 4, 2011
Structure of the response regulator PhoP from Mycobacterium tuberculosis reveals a dimer through the receiver domainSmita Menon, Shuishu WangBiochemistry|December 2, 2014
DNA consensus sequence motif for binding response regulator PhoP, a virulence regulator of Mycobacterium tuberculosisXiaoyuan He, Shuishu WangBiochemistry|February 8, 2006
Crystal structure of the pantothenate synthetase from Mycobacterium tuberculosis, snapshots of the enzyme in actionShuishu Wang, David EisenbergProtein Science : a Publication of the Protein Society|April 30, 2003
Crystal structures of a pantothenate synthetase from M. tuberculosis and its complexes with substrates and a reaction intermediateShuishu Wang, David EisenbergTrends in Microbiology|October 7, 2008
PhoP, a key player in Mycobacterium tuberculosis virulenceMichelle Ryndak, Shuishu Wang, Issar SmithScientific Reports|April 16, 2016
Structural basis of DNA sequence recognition by the response regulator PhoP in Mycobacterium tuberculosisXiaoyuan He, Liqin Wang, Shuishu WangBiochemistry|December 7, 2007
Structure of the DNA-binding domain of the response regulator PhoP from Mycobacterium tuberculosisShuishu Wang, Jean Engohang-Ndong, Issar SmithJournal of Bacteriology|December 2, 2009
The Mycobacterium tuberculosis high-affinity iron importer, IrtA, contains an FAD-binding domainMichelle B Ryndak, Shuishu Wang, Issar Smith, et al.Combinatorial Chemistry & High Throughput Screening|October 18, 2016
A High-Throughput Assay for Developing Inhibitors of PhoP, a Virulence Factor of Mycobacterium tuberculosisLiqin Wang, Miao Xu, Noel Southall, et al.FEBS Open Bio|August 8, 2017
Structure-based design of ferritin nanoparticle immunogens displaying antigenic loops of Neisseria gonorrhoeaeLiqin Wang, Daniel Xing, Adriana Le Van, et al.Pageof 7